| Literature DB >> 26188548 |
Abstract
Ugp1, a UDP-glucose pyrophosphorylase, is essential for various cellular activities in Saccharomyces cerevisiae because its product, UDP-glucose, is a sole glucosyl donor in several metabolic pathways. Here, we report that Msn2/4 play a crucial role in the regulation of UGP1 expression. Msn2/4 bound to three stress response elements in the UGP1 promoter in a protein kinase A (PKA)-dependent manner. Several stresses induced UGP1 transcription, suggesting that the regulation of UGP1 mediated by Msn2/4 is involved in general stress response. Furthermore, the phosphate response (PHO) pathway also controlled Msn2/4-dependent regulation of UGP1, providing a novel link between the PKA and PHO pathways. Our data suggest that signals of the PKA, PHO and stress response pathways regulate UGP1 expression via Msn2/4 in S. cerevisiae.Entities:
Keywords: Msn2/4; Phosphate response; Protein kinase A; Stress response; Ugp1
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Year: 2015 PMID: 26188548 DOI: 10.1016/j.febslet.2015.07.015
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124